Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

Regulator of cell cycle RGCC (Response gene to complement 32 protein) (RGC-32)

 RGCC_HUMAN              Reviewed;         137 AA.
Q9H4X1; Q6NZ48; Q9UL69;
06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
01-MAR-2001, sequence version 1.
05-JUL-2017, entry version 110.
RecName: Full=Regulator of cell cycle RGCC;
AltName: Full=Response gene to complement 32 protein;
Short=RGC-32;
Name=RGCC; Synonyms=C13orf15, RGC32;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, INDUCTION,
SUBCELLULAR LOCATION, MUTAGENESIS OF THR-111, PHOSPHORYLATION AT
THR-111, AND TISSUE SPECIFICITY.
TISSUE=Fetal brain;
PubMed=11687586; DOI=10.1074/jbc.M109354200;
Badea T., Niculescu F., Soane L., Fosbrink M., Sorana H., Rus V.,
Shin M.L., Rus H.;
"RGC-32 increases p34CDC2 kinase activity and entry of aortic smooth
muscle cells into S-phase.";
J. Biol. Chem. 277:502-508(2002).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15057823; DOI=10.1038/nature02379;
Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L.,
Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E.,
Griffiths-Jones S., Jones M.C., Keenan S.J., Oliver K., Scott C.E.,
Ainscough R., Almeida J.P., Ambrose K.D., Andrews D.T.,
Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Bannerjee R.,
Barlow K.F., Bates K., Beasley H., Bird C.P., Bray-Allen S.,
Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P.,
Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M.,
Clegg S.C., Cobley V., Collins J.E., Corby N., Coville G.J.,
Deloukas P., Dhami P., Dunham I., Dunn M., Earthrowl M.E.,
Ellington A.G., Faulkner L., Frankish A.G., Frankland J., French L.,
Garner P., Garnett J., Gilbert J.G.R., Gilson C.J., Ghori J.,
Grafham D.V., Gribble S.M., Griffiths C., Hall R.E., Hammond S.,
Harley J.L., Hart E.A., Heath P.D., Howden P.J., Huckle E.J.,
Hunt P.J., Hunt A.R., Johnson C., Johnson D., Kay M., Kimberley A.M.,
King A., Laird G.K., Langford C.J., Lawlor S., Leongamornlert D.A.,
Lloyd D.M., Lloyd C., Loveland J.E., Lovell J., Martin S.,
Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S.,
Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I.,
Pelan S., Phillimore B., Porter K.M., Rice C.M., Searle S.,
Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Steward C.A.,
Sycamore N., Tester J., Thomas D.W., Tracey A., Tromans A., Tubby B.,
Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L.,
Wilming L., Wray P.W., Wright M.W., Young L., Coulson A., Durbin R.M.,
Hubbard T., Sulston J.E., Beck S., Bentley D.R., Rogers J., Ross M.T.;
"The DNA sequence and analysis of human chromosome 13.";
Nature 428:522-528(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
TISSUE SPECIFICITY.
PubMed=15713436; DOI=10.1016/j.yexmp.2004.11.001;
Fosbrink M., Cudrici C., Niculescu F., Badea T.C., David S.,
Shamsuddin A., Shin M.L., Rus H.;
"Overexpression of RGC-32 in colon cancer and other tumors.";
Exp. Mol. Pathol. 78:116-122(2005).
[5]
INTERACTION WITH PLK1, FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=17146433; DOI=10.1038/sj.onc.1210148;
Saigusa K., Imoto I., Tanikawa C., Aoyagi M., Ohno K., Nakamura Y.,
Inazawa J.;
"RGC32, a novel p53-inducible gene, is located on centrosomes during
mitosis and results in G2/M arrest.";
Oncogene 26:1110-1121(2007).
[6]
FUNCTION.
PubMed=19158077; DOI=10.1074/jbc.M900039200;
Huang W.Y., Li Z.G., Rus H., Wang X., Jose P.A., Chen S.Y.;
"RGC-32 mediates transforming growth factor-beta-induced epithelial-
mesenchymal transition in human renal proximal tubular cells.";
J. Biol. Chem. 284:9426-9432(2009).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-69; SER-71; SER-75;
SER-97 AND THR-111, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[8]
FUNCTION, AND INDUCTION.
PubMed=22163048; DOI=10.1371/journal.pone.0028638;
Schlick S.N., Wood C.D., Gunnell A., Webb H.M., Khasnis S.,
Schepers A., West M.J.;
"Upregulation of the cell-cycle regulator RGC-32 in Epstein-Barr
virus-immortalized cells.";
PLoS ONE 6:E28638-E28638(2011).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-97, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
-!- FUNCTION: Modulates the activity of cell cycle-specific kinases.
Enhances CDK1 activity. May contribute to the regulation of the
cell cycle. May inhibit growth of glioma cells by promoting arrest
of mitotic progression at the G2/M transition. Fibrogenic factor
contributing to the pathogenesis of renal fibrosis through
fibroblast activation. {ECO:0000269|PubMed:11687586,
ECO:0000269|PubMed:17146433, ECO:0000269|PubMed:19158077,
ECO:0000269|PubMed:22163048}.
-!- SUBUNIT: Interacts with SMAD3 (By similarity). Interacts with CDK1
and PLK1. {ECO:0000250, ECO:0000269|PubMed:17146433}.
-!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cytoplasm, cytoskeleton,
microtubule organizing center, centrosome. Note=Cytoplasmic in
unstimulated cells. Nuclear after activation by complement.
Associated with the centrosome during prometaphase and metaphase.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q9H4X1-1; Sequence=Displayed;
Name=2;
IsoId=Q9H4X1-2; Sequence=VSP_022873;
-!- TISSUE SPECIFICITY: Detected in brain, heart and liver (at protein
level). Highly expressed in liver, skeletal muscle, kidney and
pancreas. Detected at lower levels in heart, brain and placenta.
Detected in aorta endothelial cells. Overexpressed in colon,
breast, prostate, bladder, lung, and ovarian cancer tissues.
{ECO:0000269|PubMed:11687586, ECO:0000269|PubMed:15713436}.
-!- INDUCTION: By Epstein-Barr virus (EBV). Up-regulated in aorta
endothelial cells in response to complement activation.
{ECO:0000269|PubMed:11687586, ECO:0000269|PubMed:22163048}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AF036549; AAF04336.1; -; mRNA.
EMBL; AL354833; CAC13101.1; -; Genomic_DNA.
EMBL; BC066334; AAH66334.1; -; mRNA.
CCDS; CCDS41880.1; -. [Q9H4X1-1]
RefSeq; NP_054778.2; NM_014059.2. [Q9H4X1-1]
UniGene; Hs.507866; -.
ProteinModelPortal; Q9H4X1; -.
SMR; Q9H4X1; -.
BioGrid; 118805; 10.
IntAct; Q9H4X1; 2.
STRING; 9606.ENSP00000368664; -.
iPTMnet; Q9H4X1; -.
PhosphoSitePlus; Q9H4X1; -.
BioMuta; RGCC; -.
DMDM; 74752653; -.
EPD; Q9H4X1; -.
MaxQB; Q9H4X1; -.
PaxDb; Q9H4X1; -.
PeptideAtlas; Q9H4X1; -.
PRIDE; Q9H4X1; -.
Ensembl; ENST00000379359; ENSP00000368664; ENSG00000102760. [Q9H4X1-1]
GeneID; 28984; -.
KEGG; hsa:28984; -.
UCSC; uc001uyi.3; human. [Q9H4X1-1]
CTD; 28984; -.
DisGeNET; 28984; -.
GeneCards; RGCC; -.
H-InvDB; HIX0011268; -.
HGNC; HGNC:20369; RGCC.
HPA; HPA035638; -.
HPA; HPA063701; -.
MIM; 610077; gene.
neXtProt; NX_Q9H4X1; -.
OpenTargets; ENSG00000102760; -.
PharmGKB; PA134895181; -.
eggNOG; ENOG410J12H; Eukaryota.
eggNOG; ENOG4111Y7V; LUCA.
GeneTree; ENSGT00390000011709; -.
HOGENOM; HOG000294092; -.
HOVERGEN; HBG060999; -.
InParanoid; Q9H4X1; -.
OMA; FRYDEHL; -.
OrthoDB; EOG091G1849; -.
PhylomeDB; Q9H4X1; -.
TreeFam; TF336312; -.
Reactome; R-HSA-6804115; TP53 regulates transcription of additional cell cycle genes whose exact role in the p53 pathway remain uncertain.
GeneWiki; C13orf15; -.
GenomeRNAi; 28984; -.
PRO; PR:Q9H4X1; -.
Proteomes; UP000005640; Chromosome 13.
Bgee; ENSG00000102760; -.
CleanEx; HS_C13orf15; -.
Genevisible; Q9H4X1; HS.
GO; GO:0005813; C:centrosome; IDA:BHF-UCL.
GO; GO:0005737; C:cytoplasm; IDA:BHF-UCL.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0005730; C:nucleolus; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:BHF-UCL.
GO; GO:0030295; F:protein kinase activator activity; IDA:BHF-UCL.
GO; GO:0019901; F:protein kinase binding; IPI:BHF-UCL.
GO; GO:0070412; F:R-SMAD binding; IPI:BHF-UCL.
GO; GO:0071456; P:cellular response to hypoxia; IMP:BHF-UCL.
GO; GO:0006956; P:complement activation; IMP:BHF-UCL.
GO; GO:0006977; P:DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest; TAS:Reactome.
GO; GO:0072537; P:fibroblast activation; ISS:UniProtKB.
GO; GO:0071850; P:mitotic cell cycle arrest; IDA:BHF-UCL.
GO; GO:0016525; P:negative regulation of angiogenesis; IDA:BHF-UCL.
GO; GO:0043537; P:negative regulation of blood vessel endothelial cell migration; IDA:BHF-UCL.
GO; GO:0008285; P:negative regulation of cell proliferation; IMP:BHF-UCL.
GO; GO:2000048; P:negative regulation of cell-cell adhesion mediated by cadherin; IDA:BHF-UCL.
GO; GO:0050710; P:negative regulation of cytokine secretion; IMP:BHF-UCL.
GO; GO:0001937; P:negative regulation of endothelial cell proliferation; IDA:BHF-UCL.
GO; GO:0001100; P:negative regulation of exit from mitosis; IDA:BHF-UCL.
GO; GO:0090272; P:negative regulation of fibroblast growth factor production; IDA:BHF-UCL.
GO; GO:1901991; P:negative regulation of mitotic cell cycle phase transition; IDA:BHF-UCL.
GO; GO:0071158; P:positive regulation of cell cycle arrest; IDA:BHF-UCL.
GO; GO:0032967; P:positive regulation of collagen biosynthetic process; IDA:BHF-UCL.
GO; GO:0031659; P:positive regulation of cyclin-dependent protein serine/threonine kinase activity involved in G1/S transition of mitotic cell cycle; IDA:BHF-UCL.
GO; GO:0050715; P:positive regulation of cytokine secretion; IMP:BHF-UCL.
GO; GO:2000573; P:positive regulation of DNA biosynthetic process; ISS:BHF-UCL.
GO; GO:2000353; P:positive regulation of endothelial cell apoptotic process; IDA:BHF-UCL.
GO; GO:0010718; P:positive regulation of epithelial to mesenchymal transition; IDA:BHF-UCL.
GO; GO:1901203; P:positive regulation of extracellular matrix assembly; IDA:BHF-UCL.
GO; GO:0003331; P:positive regulation of extracellular matrix constituent secretion; IDA:BHF-UCL.
GO; GO:0010628; P:positive regulation of gene expression; IDA:BHF-UCL.
GO; GO:0045840; P:positive regulation of mitotic nuclear division; IMP:BHF-UCL.
GO; GO:0051091; P:positive regulation of sequence-specific DNA binding transcription factor activity; IMP:BHF-UCL.
GO; GO:0051496; P:positive regulation of stress fiber assembly; IDA:BHF-UCL.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IMP:BHF-UCL.
InterPro; IPR029252; RGCC.
PANTHER; PTHR32193; PTHR32193; 1.
Pfam; PF15151; RGCC; 1.
1: Evidence at protein level;
Alternative splicing; Cell cycle; Complete proteome; Cytoplasm;
Cytoskeleton; Nucleus; Phosphoprotein; Reference proteome.
CHAIN 1 137 Regulator of cell cycle RGCC.
/FTId=PRO_0000274701.
COMPBIAS 11 26 Ala-rich.
COMPBIAS 64 109 Ser/Thr-rich.
MOD_RES 67 67 Phosphoserine.
{ECO:0000250|UniProtKB:Q9DBX1}.
MOD_RES 69 69 Phosphoserine.
{ECO:0000244|PubMed:19690332}.
MOD_RES 71 71 Phosphoserine.
{ECO:0000244|PubMed:19690332}.
MOD_RES 75 75 Phosphoserine.
{ECO:0000244|PubMed:19690332}.
MOD_RES 91 91 Phosphoserine.
{ECO:0000250|UniProtKB:Q9Z2P4}.
MOD_RES 97 97 Phosphoserine.
{ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:23186163}.
MOD_RES 111 111 Phosphothreonine; by CDK1.
{ECO:0000244|PubMed:19690332,
ECO:0000269|PubMed:11687586}.
VAR_SEQ 6 25 Missing (in isoform 2).
{ECO:0000303|PubMed:11687586}.
/FTId=VSP_022873.
MUTAGEN 111 111 T->A: Loss of phosphorylation. Reduced
stimulation of CDK1 activity.
{ECO:0000269|PubMed:11687586}.
CONFLICT 3 3 P -> Q (in Ref. 3; AAH66334).
{ECO:0000305}.
SEQUENCE 137 AA; 14559 MW; 76265677DBCD9525 CRC64;
MKPPAAQGSP AAAAAAAPAL DSAAAEDLSD ALCEFDAVLA DFASPFHERH FHYEEHLERM
KRRSSASVSD SSGFSDSESA DSLYRNSFSF SDEKLNSPTD STPALLSATV TPQKAKLGDT
KELEAFIADL DKTLASM


Related products :

Catalog number Product name Quantity
27-305 In response to DNA damage and replication blocks, cell cycle progression is halted through the control of critical cell cycle regulators. CHEK2 is a cell cycle checkpoint regulator and putative tumor 0.05 mg
27-302 RAD17 is highly similar to the gene product of Schizosaccharomyces pombe rad17, a cell cycle checkpoint gene required for cell cycle arrest and DNA damage repair in response to DNA damage. This protei 0.1 mg
30-841 HUS1Bis most closely related to HUS1, a component of a cell cycle checkpoint protein complex involved in cell cycle arrest in response to DNA damage. HUS1B can interact with the check point protein RA 0.05 mg
EIAAB05873 CARP1,CARP-1,CCAR1,Cell cycle and apoptosis regulatory protein 1,Cell division cycle and apoptosis regulator protein 1,Death inducer with SAP domain,DIS,Homo sapiens,Human
EIAAB05874 Carp1,CARP-1,Ccar1,Cell cycle and apoptosis regulatory protein 1,Cell division cycle and apoptosis regulator protein 1,Mouse,Mus musculus
CCAR1_HUMAN ELISA Kit FOR Cell division cycle and apoptosis regulator protein 1; organism: Human; gene name: CCAR1 96T
CCAR1_MOUSE ELISA Kit FOR Cell division cycle and apoptosis regulator protein 1; organism: Mouse; gene name: Ccar1 96T
CCBL1 CCAR1 Gene cell division cycle and apoptosis regulator 1
M89BB_HUMAN ELISA Kit FOR Cell cycle regulator Mat89Bb homolog; organism: Human; gene name: C12orf11 96T
RGC32_RAT ELISA Kit FOR Response gene to complement 32 protein; organism: Rat; gene name: Rgc32 96T
15-288-21301 Regulator of G-protein signaling 1 - RGS1; Early response protein 1R20; B-cell activation protein BL34 Polyclonal 0.05 mg
15-288-21301 Regulator of G-protein signaling 1 - RGS1; Early response protein 1R20; B-cell activation protein BL34 Polyclonal 0.1 mg
RGC32_MOUSE ELISA Kit FOR Response gene to complement 32 protein; organism: Mouse; gene name: Rgc32 96T
CSB-EL004614MO Mouse Cell division cycle and apoptosis regulator protein 1(CCAR1) ELISA kit 96T
CSB-EL004614HU Human Cell division cycle and apoptosis regulator protein 1(CCAR1) ELISA kit 96T
CSB-EL004614MO Mouse Cell division cycle and apoptosis regulator protein 1(CCAR1) ELISA kit SpeciesMouse 96T
CSB-EL004614HU Human Cell division cycle and apoptosis regulator protein 1(CCAR1) ELISA kit SpeciesHuman 96T
25-771 GTSE1 is only expressed in the S and G2 phases of the cell cycle, where it colocalizes with cytoplasmic tubulin and microtubules. In response to DNA damage, the encoded protein accumulates in the nucl 0.05 mg
25-772 GTSE1 is only expressed in the S and G2 phases of the cell cycle, where it colocalizes with cytoplasmic tubulin and microtubules. In response to DNA damage, the encoded protein accumulates in the nucl 0.05 mg
G7289 Response gene to complement 32 protein (C13orf15), Human, ELISA Kit 96T
CSB-EL003110HU Human Response gene to complement 32 protein(C13orf15) ELISA kit 96T
EIAAB34462 Mouse,Mus musculus,Response gene to complement 32 protein,Rgc32,RGC-32
EIAAB34463 Rat,Rattus norvegicus,Response gene to complement 32 protein,Rgc32,RGC-32
26-109 DLG7 is a potential cell cycle regulator that may play a role in carcinogenesis of cancer cells. It is a mitotic phosphoprotein regulated by the ubiquitin-proteasome pathway. DLG7 is the key regulator 0.05 mg
25-602 CDC5L shares a significant similarity with Schizosaccharomyces pombe cdc5 gene product, which is a cell cycle regulator important for G2_M transition. CDC5L has been demonstrated to act as a positive 0.05 mg


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur